Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center
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Drug-induced reactivation of apoptosis abrogates HIV-1 infectionEvolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sitesRevisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.Functional significance of eIF5A and its hypusine modification in eukaryotesIron chaperones PCBP1 and PCBP2 mediate the metallation of the dinuclear iron enzyme deoxyhypusine hydroxylase.Special delivery: distributing iron in the cytosol of mammalian cells.Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexesA family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis.Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates H(peroxo) and Q proceed by distinct mechanismsAdvances in iron chelation: an update.A unique modification of the eukaryotic initiation factor 5A shows the presence of the complete hypusine pathway in Leishmania donovani.Mössbauer, electron paramagnetic resonance, and density functional theory studies of synthetic S = 1/2 Fe(III)-O-Fe(IV)═O complexes. Superexchange-mediated spin transition at the Fe(IV)═O site.Cofactor biosynthesis through protein post-translational modification.Dioxygen activation in soluble methane monooxygenaseCyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins.Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylaseToward functional carboxylate-bridged diiron protein mimics: achieving structural stability and conformational flexibility using a macrocylic ligand frameworkAssay of deoxyhypusine hydroxylase activity.Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.Substrate-triggered activation of a synthetic [Fe2(μ-O)2] diamond core for C-H bond cleavage.Structure of the key species in the enzymatic oxidation of methane to methanolStructural, EPR, and Mössbauer characterization of (μ-alkoxo)(μ-carboxylato)diiron(II,III) model complexes for the active sites of mixed-valent diiron enzymes.Protonation of a peroxodiiron(III) complex and conversion to a diiron(III/IV) intermediate: implications for proton-assisted O-O bond cleavage in nonheme diiron enzymes.Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox PartnersParallel and competitive pathways for substrate desaturation, hydroxylation, and radical rearrangement by the non-heme diiron hydroxylase AlkB.Dioxygen and nitric oxide scavenging by Treponema denticola flavodiiron protein: a mechanistic paradigm for catalysisAging-associated enzyme human clock-1: substrate-mediated reduction of the diiron center for 5-demethoxyubiquinone hydroxylation.Hydrogen-bonding effects on the reactivity of [X-Fe(III)-O-Fe(IV)═O] (X = OH, F) complexes toward C-H bond cleavage.Current status of the polyamine research fieldFactors affecting the carboxylate shift upon formation of nonheme diiron-O2 adducts.Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate.Roles of eukaryotic initiation factor 5A2 in human cancer.Modifying the maker: Oxygenases target ribosome biology.Structure/function correlations over binuclear non-heme iron active sitesDivergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway.New insights into novel inhibitors against deoxyhypusine hydroxylase from plasmodium falciparum: compounds with an iron chelating potential.X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5aAn Iron(II)(1,3-bis(2'-pyridylimino)isoindoline) Complex as a Catalyst for Substrate Oxidation with H2O2. Evidence for a Transient Peroxodiiron(III) Species.
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P2860
Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 19 August 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Human deoxyhypusine hydroxylas ...... 2 with a nonheme diiron center
@en
Human deoxyhypusine hydroxylas ...... with a nonheme diiron center.
@nl
type
label
Human deoxyhypusine hydroxylas ...... 2 with a nonheme diiron center
@en
Human deoxyhypusine hydroxylas ...... with a nonheme diiron center.
@nl
prefLabel
Human deoxyhypusine hydroxylas ...... 2 with a nonheme diiron center
@en
Human deoxyhypusine hydroxylas ...... with a nonheme diiron center.
@nl
P2093
P2860
P50
P356
P1476
Human deoxyhypusine hydroxylas ...... 2 with a nonheme diiron center
@en
P2093
Eckard Münck
Lawrence Que
Myung Hee Park
Yeon Sook Kim
P2860
P304
14814-14819
P356
10.1073/PNAS.0904553106
P407
P577
2009-08-19T00:00:00Z